ID A0A286UF06_9AGAM Unreviewed; 1482 AA.
AC A0A286UF06;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=PNOK_0657100 {ECO:0000313|EMBL:PAV18085.1};
OS Pyrrhoderma noxium.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Hymenochaetales; Hymenochaetaceae; Pyrrhoderma.
OX NCBI_TaxID=2282107 {ECO:0000313|EMBL:PAV18085.1, ECO:0000313|Proteomes:UP000217199};
RN [1] {ECO:0000313|Proteomes:UP000217199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FFPRI411160 {ECO:0000313|Proteomes:UP000217199};
RA Chung C.-L., Lee J.T., Akiba M., Lee H.-H., Kuo T.-H., Liu D., Ke H.-M.,
RA Yokoi T., Roa M.B., Lu M.J., Chang Y.-Y., Ann P.-J., Tsai J.-N.,
RA Chen C.-Y., Tzean S.-S., Ota Y., Hattori T., Sahashi N., Liou R.-F.,
RA Kikuchi T., Tsai I.J.;
RT "The Genomic Landscape Of Tree Rot In Phellinus noxius And Its
RT Hymenochaetales Members.";
RL bioRxiv 0:0-0(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAV18085.1}.
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DR EMBL; NBII01000006; PAV18085.1; -; Genomic_DNA.
DR STRING; 2282107.A0A286UF06; -.
DR InParanoid; A0A286UF06; -.
DR OrthoDB; 3249969at2759; -.
DR Proteomes; UP000217199; Chromosome 6.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 2.
DR CDD; cd05811; CBM20_glucoamylase; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR034836; CBM20_glucoamylase.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR010905; Glyco_hydro_88.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 2.
DR Pfam; PF02806; Alpha-amylase_C; 2.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF07470; Glyco_hydro_88; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 2.
DR SMART; SM00632; Aamy_C; 2.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 2.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PAV18085.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000217199};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1482
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013574946"
FT DOMAIN 870..972
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 1344..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1482 AA; 160322 MW; 55523862AC42D221 CRC64;
MTKVAGFLTF LSLHFILVLA APKPPAGSYA KWAADSGIAR GQGNGSVNGV PAVSYEHGEF
QWALRLLYEA TGNQSYYDYI KYGVDTVLSE DGKTISGYNV SEFQLDPLRV GPSFIYLHET
TKEQKYKSAA DVFRAQLDSH PRTEAGQFWH KLRYPNQGWL DGIYMGDIFY AHYTSAYEKD
NQSAWEDINK QLTLMYENTI QLPSDANYTG LLYHGYDASD TAVWASSDRG HSPEVWDRAD
GWFLMSLVDF LEFVPASQPL HTSALSQLCN LIPRVLSQAD PAWWLVITEP GREGNYFESS
GAAMFVYSLL KAVRLGFVED LDGRIIQVAL DAYRYMIEHW VTANDDGTMS WEGTVHVGSL
DLAGDFDYYI AQSVDTNDLK GLAAFNAVGK HSGLKPRSQS FHRTDSTPHG LFPAPSASKD
VIIQMFEWSW DSIAAECTNF IGPAGYGFIQ ASPAQETITG DQWWTDYQPV SYILTGKRGD
RSQYQNMINT CHAAGVKVIA DTIFNHMTGE DSGTGTAGSS FTHYVYPGIY QYQDFHHCGL
EPNDDIVNYD NRLEVQTCQL VGLADLATDT EYVRSRLAEY GNDLLSLGVD GMRLDAAKHI
AATDLANITS RLNGAPYLTQ EVIYGAGEPI TPAEYVGIGD VQEFRYTTAV KNGFLSDGIS
GLQNLDNQGW VSGSVANVFV ANHDTERNGN SLNSNSPSNA YTLAMIFSLA HPYGTPTILS
SYSFSDTDAG SPNSGTGSCS TDGGSNGWLC QHRWPAVVGM LGFRNTVRGT SSNALSNWVS
PSSNQIAFSR GSVAFVAINN EDSSWTAEFN TGLPEGEYCD VIAGAPQTAG TCRGQSFNVS
STGTFSTTIS ARNAVAIHIG ALGTGDNTGT SNGGSATVIF QETATTVFGE NIFLVGSISQ
LGSWNTAQAL ALSAATYPVW ALTVSLPAST TFEYKFIRVE SDGSIEWESD PNRSLTTGSS
GTTQTVQTTW RSGALNTSGL RSLELIVLLY LPDVIIQMFE WDWDSIASEC TNFIGPTGYG
YVQISPTQEH VEGDQWWTDY QPITYNLTSK RGNRDQLKKL IDTCHAAGVK VIADTVFNHM
SSMDSGKGVA GTPFTHYEYA GIYGYDDFHH CGLEPYDTIV DSSNLKELQT CQLANLSDLA
TEKDYVQSRL AEHGNDLIGM GVDGFRLDSA KLIADSELAS ITGRLTGSPY ITQEIIITEG
DTNTSALYSK IGDIQEFRYT TALMNAFAKG AGIQDLEQLD NRGWVPSDIA NVFVANHDTE
RKGTSLNNNS QSNTYELAMI FSLAHSYGTP TILSSYTGFG DAGAPNGGAG TCNEDGSGSN
GWICQHRWPA IAGMVGFRNA IHNSTSSSSS TPDLSSNQTA VTDTSTPSNT SSSNSTSSGP
PITKWYAPTV DRVAFARGKV GFIAINNGDT PWTEEFDTGG LPQGKYCDII AGPSLNGSCK
GQTFDVSDTG KFTATVALRK AIAIHTGAMS SGNGSSDLGT PA
//
